Denaturation and change in sulfhydryl group of actomyosin from milkfish (Chanos chanos) during storage at -20.degree.C

Differences in properties of myofibrillar proteins from bovine semitendinosus muscle after hydrostatic pressure or heat treatment

“…Ca‐ and Mg‐ATPase activities were determined by a modification of the method of Jiang et al 19 Ca‐ATPase activities of HP‐treated Mf were measured in a reaction mixture containing 5 mmol L −1 CaCl 2 , 100 mmol L −1 KCl, 25 mmol L −1 Tris‐maleate (pH 7; shows maximum ATPase activity20), 1 mmol L −1 ATP and 5 mg mL −1 protein at 25°C. Similarly, Mg‐ATPase activities were measured in 2 mmol L −1 MgCl 2 , 100 mmol L −1 KCl, 25 mmol L −1 Tris‐maleate (pH 7), 1 mmol L −1 ATP and 5 mg mL −1 protein at 25°C.…”

Utilization of freeze-dried mackerel (Scomber australasicus) muscle proteins as a binder in restructured meat

“…Low extractable AM in thawed fish might be due to the freeze‐denaturation of myofibrillar proteins during frozen storage. 49–54 The extractable AM of fish sol was higher than that of thawed fish due to the removal of water‐soluble protein during the washing treatment, which consequently increased the relative ratio of extractable AM of fish sol to that of fish meat. Although 3% sugar was added to prevent the denaturation of myofibrillar proteins, the AM extractability of fish sol decreased immediately after freezing and further decreased after freeze‐drying processing ( Table 1).…”

“…The reducing agents and sulfide reductase have been thought to be able to reduce the disulfide bonds to SH group. 51–53,55,56 …”

“…Low extractable AM in thawed fish might be due to the freeze-denaturation of myofibrillar proteins during frozen storage. [49][50][51][52][53][54] The extractable AM of fish sol was higher than that of thawed fish due to the removal of watersoluble protein during the washing treatment, which consequently increased the relative ratio of extractable quality meat binders. The objectives of this study were to evaluate the potential for making meat binders using freeze-thawed mackerel (Scomber australasicus), and to determine the effects of different reducing agents on the protein quality and binding ability of the meat binder.…”

Textural and Microstructural Changes in Frozen Stored Sardine Mince Gels

“…A more likely explanation would be an increase in the degree of insolubilization resulting from the predominance of bonds stronger than hydrophobic interactions. In this connection Jiang et al (1988) reported the formation of disulfide bonds in milkfish actomyosin during freezing and frozen storage. However, the possible increase in Table 3-Soluble protein (SP) in S1 and S2 gels frozen (F) at Ϫ40 or Ϫ18؇C and stored (S) at Ϫ18 or Ϫ12؇C S-S bonds did not bring about an increase in shear strength by the end of storage since, the gel matrix had been completely disrupted by large numbers of cavities.…”